IndraLab

Statements


USP13 deubiquitinates USP10. 8 / 9
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"As previously mentioned, USP10 mediates the deubiquitination of Beclin1, and USP13 can directly regulate the deubiquitination of USP10 to promote the formation of autophagosomes ."

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"A previous study indicated that USP13 affects p53 by deubiquitinating USP10 [33]."

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"Consistent with this possibility, the ubiquitination levels of USP10 were reduced when cells were cotransfected with an expression vector of USP13 and the addition of spautin-1 inhibited the deubiquitination of USP10 by USP13 (XREF_FIG)."

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"These results suggest that USP13 may directly regulate the deubiquitination of USP10; however, USP10 may regulate USP13 indirectly perhaps by affecting the levels of Vps34 complexes."

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"Moreover, beclin-1 and USP10 are involved in a potential feedforward mechanism in which beclin-1 stabilizes USP13, which in turn deubiquitinates and stabilizes USP10, leading to increased beclin-1 levels and activity."

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"Since USP13 can also deubiquitinate USP10, regulating the stability of USP13 by Beclin1 provides a mechanism for Beclin1 to control the stability of USP10."

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"Very interestingly, they also pointed out that beclin-1 controlled the stability of USP10 by regulating the stability of USP13, which can deubiquitinate USP10 (also see Figure 4) [53]."

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"USP13 has been found to stabilize p53, a typical tumor suppressor by de-ubiquitinating its de-ubiquitinating protease USP10 [24]."